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Isolation of a Peptide That Binds to Pseudomonas aeruginosa Lytic Bacteriophage
Soo Khim Chan1, Zhongchao Zhao1, Samuel Penziner1
1Department of NanoEngineering, Department of Medicine, Department of Pathology, Department of Bioengineering, Department of Radiology, Center for Nano-ImmunoEngineering, Moores Cancer Center, and Institute for Materials Discovery and Design, University of California San Diego, 9500 Gilman Dr., La Jolla, California 92093, United States.
Abstract:
Antimicrobial resistance is a global health threat that is exacerbated by the overuse and misuse of antibiotics in medicine and agriculture. As an alternative to conventional antimicrobial drugs, phage therapy involves the treatment of infected patients with a bacteriophage that naturally destroys bacterial pathogens. With the re-emergence of phage therapy, novel tools are needed to study phages. In this work we set out to screen and isolate peptide candidates that bind to phages and act as affinity tags. Such peptides functionalized with an imaging agent could serves as versatile tools for tracking and imaging of phages. Specifically, we screened a phage display library for peptides that bind to the Good Vibes phage (GV), which lyses the bacterial pathogen Pseudomonas aeruginosa. Isolated monoclonal library phages featured a highly conserved consensus motif, LPPIXRX. The corresponding peptide WDLPPIGRLSGN was synthesized with a GGGSK linker and conjugated to cyanine 5 or biotin. The specific binding of the LPPIXRX motif to GV in vitro was confirmed using an enzyme-linked immunosorbent assay. We demonstrated imaging and tracking of GV in bacterial populations using the fluorescent targeting peptide and flow cytometry. In conclusion, we developed fluorescent labeled peptides that can bind to bacteriophage GV specifically, which may enable real-time analysis of phage in vivo and monitor the efficacy of phage therapy.
Insights
Researchers developed fluorescent peptides to track bacteriophages, a promising alternative to antibiotics. These peptides specifically bind to the Good Vibes phage, aiding in real-time monitoring of phage therapy effectiveness against bacterial infections.
Area of Science:
- Biotechnology
- Microbiology
- Molecular Biology
Background:
- Antimicrobial resistance is a growing global health crisis, driving the need for alternative treatments like phage therapy.
- Phage therapy utilizes bacteriophages to combat bacterial pathogens, but requires advanced tools for effective study and application.
- Current methods for tracking bacteriophages are limited, hindering the optimization and monitoring of phage therapy.
Purpose of the Study:
- To screen and isolate peptides that specifically bind to bacteriophages, serving as affinity tags.
- To develop novel imaging tools for tracking and visualizing bacteriophages in real-time.
- To create functionalized peptides for monitoring phage behavior and therapeutic efficacy.
Main Methods:
- Screening a phage display library to identify peptides binding to the Good Vibes phage (GV).
- Synthesizing and conjugating the identified peptide motif (LPPIXRX) with imaging agents (cyanine 5 or biotin).
- Confirming specific peptide-phage binding using enzyme-linked immunosorbent assays and demonstrating imaging via flow cytometry.
Main Results:
- A conserved consensus motif (LPPIXRX) was identified in peptides binding to the Good Vibes phage.
- Fluorescently labeled peptides specifically bound to the Good Vibes phage, confirmed by in vitro assays.
- The labeled peptides enabled successful imaging and tracking of bacteriophages within bacterial populations.
Conclusions:
- Developed fluorescently labeled peptides that specifically bind to bacteriophage GV.
- These peptides can serve as versatile tools for real-time in vivo analysis of phages.
- Potential to significantly enhance the monitoring and efficacy assessment of phage therapy.
